ArticlePloS one2012
Structure-function analysis of human TYW2 enzyme required for the biosynthesis of a highly modified Wybutosine (yW) base in phenylalanine-tRNA.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Molecular basis of tRNA aminocarboxypropyl-transferase TapT for substrate recognition.Nucleic acids research · 2025Article
- Translation dysregulation in cancer as a source for targetable antigens.Cancer cell · 2025Article
- CIMT 2024: Report on the 21st Annual Meeting of the Association for Cancer Immunotherapy.Human vaccines & immunotherapeutics · 2024Article
- Human transfer RNA modopathies: diseases caused by aberrations in transfer RNA modifications.The FEBS journal · 2021Review
- The expanding world of tRNA modifications and their disease relevance.Nature reviews. Molecular cell biology · 2021Review
- The nature of the modification at position 37 of tRNAPhe correlates with acquired taxol resistance.Nucleic acids research · 2021Article
- Biochemical Pathways Leading to the Formation of Wyosine Derivatives in tRNA of Archaea.Biomolecules · 2020Review
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- The life history of retrocopies illuminates the evolution of new mammalian genes.Genome research · 2016Article
- Structural and functional studies of S-adenosyl-L-methionine binding proteins: a ligand-centric approach.BMC structural biology · 2013Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Posttranscriptional modifications are critical for structure and function of tRNAs. Wybutosine (yW) and its derivatives are hyper-modified guanosines found at the position 37 of eukaryotic and archaeal tRNA(Phe). TYW2 is an enzyme that catalyzes α-amino-α-carboxypropyl transfer activity at the third step of yW biogenesis. Using complementation of a ΔTYW2 strain, we demonstrate here that human TYW2 (hTYW2) is active in yeast and can synthesize the yW of yeast tRNA(Phe). Structure-guided analysis identified several conserved residues in hTYW2 that interact with S-adenosyl-methionine (AdoMet), and mutation studies revealed that K225 and E265 are critical residues for the enzymatic activity. We previously reported that the human TYW2 is overexpressed in breast cancer. However, no difference in the tRNA(Phe) modification status was observed in either normal mouse tissue or a mouse tumor model that overexpresses Tyw2, indicating that hTYW2 may have a role in tumorigenesis unrelated to yW biogenesis.
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